Complexation ability of homologous series of amphiphiles bearing imidazolium and urethane moieties (IAC-n, n = 14, 16, 18) toward bovine serum albumin (BSA) has been investigated by various physico-chemical methods (tensiometry, fluorescence spectroscopy, spectrophotometry, dynamic and electrophoretic light scattering, circular dichroism, and transmission electron microscopy). It has been revealed, that aggregation thresholds of systems based on IAC-n could be 5–8-fold reduced by BSA addition. Fluorescent analysis allows to estimate that binding of components is favorably mediated by tryptophan amino acid residue and is driven by different forces depending on the length of amphiphile hydrophobic tail. In particular, dominate contribution of Van der Waals interactions to the complexation have been shown in the case of IAC-14 and IAC-16, while hydrophobic interactions prevailed for IAC-18. It has been demonstrated that amphiphile addition causes reversible unfolding of protein macromolecules in all cases. Spectrophotometry assay exhibits that amphiphile/BSA complexes have more significant solubilization capacity toward hydrophobic guest in comparison with individual IAC-n systems.

通过各种物理化学方法（张力测定法，荧光光谱法，分光光度法，动力学法）研究了带有咪唑鎓和氨基甲酸酯部分（IAC-n，n = 14、16、18）的两亲同源系列对牛血清白蛋白（BSA）的络合能力。电泳光散射，圆二色性和透射电子显微镜）。已经发现，通过添加BSA可以将基于IAC-n的系统的聚合阈值降低5-8倍。荧光分析允许估计组分的结合有利地由色氨酸氨基酸残基介导并且由不同的力驱动，这取决于两亲性疏水尾的长度。特别是在IAC-14和IAC-16的情况下，范德华相互作用对络合物的主要贡献已得到证实，而IAC-18则以疏水相互作用为主。已经证明，在所有情况下，添加两亲物都会引起蛋白质大分子的可逆展开。分光光度法测定表明，与单独的IAC-n系统相比，两亲/ BSA复合物对疏水性客体具有更显着的增溶能力。